PPE1_HUMAN
ID PPE1_HUMAN Reviewed; 653 AA.
AC O14829; A6NHP4; A8K348; O15253; Q9NU21; Q9UJH0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Serine/threonine-protein phosphatase with EF-hands 1;
DE Short=PPEF-1;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase with EF calcium-binding domain;
DE Short=PPEF;
DE AltName: Full=Serine/threonine-protein phosphatase 7;
DE Short=PP7;
GN Name=PPEF1; Synonyms=PPEF, PPP7C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=9326663; DOI=10.1073/pnas.94.21.11639;
RA Sherman P.M., Sun H., Macke J.P., Williams J., Smallwood P.M., Nathans J.;
RT "Identification and characterization of a conserved family of protein
RT serine/threonine phosphatases homologous to Drosophila retinal degeneration
RT C.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11639-11644(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND VARIANT THR-367.
RC TISSUE=Fetal brain;
RX PubMed=9215685; DOI=10.1093/hmg/6.7.1137;
RA Montini E., Rugarli E.I., van de Vosse E., Andolfi G., Mariani M.,
RA Puca A.A., Consales G.G., den Dunnen J.T., Ballabio A., Franco B.;
RT "A novel human serine-threonine phosphatase related to the Drosophila
RT retinal degeneration C (rdgC) gene is selectively expressed in sensory
RT neurons of neural crest origin.";
RL Hum. Mol. Genet. 6:1137-1145(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=9430683; DOI=10.1074/jbc.273.3.1462;
RA Huang X., Honkanen R.E.;
RT "Molecular cloning, expression, and characterization of a novel human
RT serine/threonine protein phosphatase, PP7, that is homologous to Drosophila
RT retinal degeneration C gene product (rdgC).";
RL J. Biol. Chem. 273:1462-1468(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
CC -!- FUNCTION: May have a role in the recovery or adaptation response of
CC photoreceptors. May have a role in development.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by calcium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0.;
CC -!- INTERACTION:
CC O14829; O43865: AHCYL1; NbExp=3; IntAct=EBI-2931238, EBI-2371423;
CC O14829; P62158: CALM3; NbExp=2; IntAct=EBI-2931238, EBI-397435;
CC O14829; P27797: CALR; NbExp=3; IntAct=EBI-2931238, EBI-1049597;
CC O14829; P36957: DLST; NbExp=3; IntAct=EBI-2931238, EBI-351007;
CC O14829; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-2931238, EBI-1055945;
CC O14829; P62204: Calm3; Xeno; NbExp=2; IntAct=EBI-2931238, EBI-397460;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=O14829-1; Sequence=Displayed;
CC Name=1A;
CC IsoId=O14829-2; Sequence=VSP_005098;
CC Name=1B;
CC IsoId=O14829-3; Sequence=VSP_005099;
CC Name=2;
CC IsoId=O14829-4; Sequence=VSP_005100, VSP_005101;
CC Name=3;
CC IsoId=O14829-5; Sequence=VSP_005102;
CC -!- TISSUE SPECIFICITY: Detected in retina and retinal derived Y-79
CC retinoblastoma cells. Also found in fetal brain.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May have no functional significance.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF023455; AAB82795.1; -; mRNA.
DR EMBL; X97867; CAA66461.1; -; mRNA.
DR EMBL; AF027977; AAC05825.1; -; mRNA.
DR EMBL; AK290463; BAF83152.1; -; mRNA.
DR EMBL; AL096700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z94056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98944.1; -; Genomic_DNA.
DR EMBL; BC036026; AAH36026.1; -; mRNA.
DR CCDS; CCDS14188.1; -. [O14829-1]
DR CCDS; CCDS43920.1; -. [O14829-5]
DR RefSeq; NP_006231.2; NM_006240.2. [O14829-1]
DR RefSeq; NP_689410.1; NM_152224.1. [O14829-3]
DR RefSeq; NP_689412.1; NM_152226.1. [O14829-5]
DR RefSeq; XP_005274610.1; XM_005274553.2.
DR AlphaFoldDB; O14829; -.
DR SMR; O14829; -.
DR BioGRID; 111471; 51.
DR IntAct; O14829; 52.
DR MINT; O14829; -.
DR STRING; 9606.ENSP00000354871; -.
DR DEPOD; PPEF1; -.
DR iPTMnet; O14829; -.
DR PhosphoSitePlus; O14829; -.
DR BioMuta; PPEF1; -.
DR MassIVE; O14829; -.
DR PaxDb; O14829; -.
DR PeptideAtlas; O14829; -.
DR PRIDE; O14829; -.
DR ProteomicsDB; 48261; -. [O14829-1]
DR ProteomicsDB; 48262; -. [O14829-2]
DR ProteomicsDB; 48263; -. [O14829-3]
DR ProteomicsDB; 48264; -. [O14829-4]
DR ProteomicsDB; 48265; -. [O14829-5]
DR Antibodypedia; 24151; 168 antibodies from 23 providers.
DR DNASU; 5475; -.
DR Ensembl; ENST00000349874.10; ENSP00000341892.5; ENSG00000086717.19. [O14829-5]
DR Ensembl; ENST00000361511.9; ENSP00000354871.3; ENSG00000086717.19. [O14829-1]
DR Ensembl; ENST00000470157.2; ENSP00000419273.2; ENSG00000086717.19. [O14829-1]
DR Ensembl; ENST00000471570.6; ENSP00000509623.1; ENSG00000086717.19. [O14829-1]
DR Ensembl; ENST00000689646.1; ENSP00000509616.1; ENSG00000086717.19. [O14829-1]
DR Ensembl; ENST00000692488.1; ENSP00000510505.1; ENSG00000086717.19. [O14829-1]
DR GeneID; 5475; -.
DR KEGG; hsa:5475; -.
DR MANE-Select; ENST00000470157.2; ENSP00000419273.2; NM_001377996.1; NP_001364925.1.
DR UCSC; uc004cyq.4; human. [O14829-1]
DR CTD; 5475; -.
DR DisGeNET; 5475; -.
DR GeneCards; PPEF1; -.
DR HGNC; HGNC:9243; PPEF1.
DR HPA; ENSG00000086717; Group enriched (brain, testis).
DR MIM; 300109; gene.
DR neXtProt; NX_O14829; -.
DR OpenTargets; ENSG00000086717; -.
DR PharmGKB; PA33564; -.
DR VEuPathDB; HostDB:ENSG00000086717; -.
DR eggNOG; KOG0377; Eukaryota.
DR GeneTree; ENSGT00940000159830; -.
DR HOGENOM; CLU_012603_1_0_1; -.
DR InParanoid; O14829; -.
DR OMA; SHDNEIN; -.
DR PhylomeDB; O14829; -.
DR TreeFam; TF313342; -.
DR PathwayCommons; O14829; -.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR SignaLink; O14829; -.
DR BioGRID-ORCS; 5475; 10 hits in 699 CRISPR screens.
DR ChiTaRS; PPEF1; human.
DR GeneWiki; PPEF1; -.
DR GenomeRNAi; 5475; -.
DR Pharos; O14829; Tbio.
DR PRO; PR:O14829; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O14829; protein.
DR Bgee; ENSG00000086717; Expressed in sperm and 118 other tissues.
DR ExpressionAtlas; O14829; baseline and differential.
DR Genevisible; O14829; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR013235; PPP_dom.
DR InterPro; IPR012008; Ser/Thr-Pase_EF-hand_contain.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR PIRSF; PIRSF000912; PPEF; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Protein phosphatase; Reference proteome; Repeat.
FT CHAIN 1..653
FT /note="Serine/threonine-protein phosphatase with EF-hands
FT 1"
FT /id="PRO_0000058899"
FT DOMAIN 16..45
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 483..518
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 566..601
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 606..641
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 121..455
FT /note="Catalytic"
FT ACT_SITE 234
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 583
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 590
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 619
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 621
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 625
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 630
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 79..132
FT /note="Missing (in isoform 1A)"
FT /evidence="ECO:0000305"
FT /id="VSP_005098"
FT VAR_SEQ 328..355
FT /note="Missing (in isoform 1B)"
FT /evidence="ECO:0000305"
FT /id="VSP_005099"
FT VAR_SEQ 356..417
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005102"
FT VAR_SEQ 356..376
FT /note="IIDILWSDPRGKNGCFPNTCR -> SGYYGKQRHQDIKRESDFTKK (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005100"
FT VAR_SEQ 377..653
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005101"
FT VARIANT 367
FT /note="K -> T (in dbSNP:rs1065074)"
FT /evidence="ECO:0000269|PubMed:9215685"
FT /id="VAR_051736"
FT VARIANT 443
FT /note="G -> S (in dbSNP:rs11796620)"
FT /id="VAR_051737"
SQ SEQUENCE 653 AA; 75792 MW; DF7B78C444EE6484 CRC64;
MGCSSSSTKT RRSDTSLRAA LIIQNWYRGY KARLKARQHY ALTIFQSIEY ADEQGQMQLS
TFFSFMLENY THIHKEELEL RNQSLESEQD MRDRWDYVDS IDVPDSYNGP RLQFPLTCTD
IDLLLEAFKE QQILHAHYVL EVLFETKKVL KQMPNFTHIQ TSPSKEVTIC GDLHGKLDDL
FLIFYKNGLP SERNPYVFNG DFVDRGKNSI EILMILCVSF LVYPNDLHLN RGNHEDFMMN
LRYGFTKEIL HKYKLHGKRI LQILEEFYAW LPIGTIVDNE ILVIHGGISE TTDLNLLHRV
ERNKMKSVLI PPTETNRDHD TDSKHNKVGV TFNAHGRIKT NGSPTEHLTE HEWEQIIDIL
WSDPRGKNGC FPNTCRGGGC YFGPDVTSKI LNKYQLKMLI RSHECKPEGY EICHDGKVVT
IFSASNYYEE GSNRGAYIKL CSGTTPRFFQ YQVTKATCFQ PLRQRVDTME NSAIKILRER
VISRKSDLTR AFQLQDHRKS GKLSVSQWAF CMENILGLNL PWRSLSSNLV NIDQNGNVEY
MSSFQNIRIE KPVQEAHSTL VETLYRYRSD LEIIFNAIDT DHSGLISVEE FRAMWKLFSS
HYNVHIDDSQ VNKLANIMDL NKDGSIDFNE FLKAFYVVHR YEDLMKPDVT NLG
